Tryptophan to phenylalanine substitutions allow differentiation of short- and long-range conformational changes during denaturation of goat α-lactalbumin

Proteins: Structure, Function and Genetics

Volumn 60, Issue 1, 2005, Pages 118-130

  Vanhooren, Ann ^a   Chedad, Allel ^a   Farkas, Viktor ^b   Majer, Zsuzsa ^b   Joniau, Marcel ^a   Van Dael, Herman ^a   Hanssens, Ignace ^a  

^a UNIVERSITY OF LEUVEN   (Belgium)

^b EÖTVÖS LORÁND UNIVERSITY   (Hungary)

Author keywords

Chemical unfolding; Circular dichroism; Differential scanning calorimetry; Fluorescence; Protein folding; Stopped flow kinetics; Thermal unfolding; Trp Phe mutants

Indexed keywords

ALPHA LACTALBUMIN; PHENYLALANINE; TRYPTOPHAN;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; ENERGY; FLOW KINETICS; NONHUMAN; PICHIA PASTORIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STABILITY; ROOM TEMPERATURE; SPECTROFLUOROMETRY; THERMAL ANALYSIS;

AMINO ACID SUBSTITUTION; ANIMALS; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; GOATS; KINETICS; LACTALBUMIN; MILK; MUTATION; PHENYLALANINE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; TEMPERATURE; THERMODYNAMICS; TRYPTOPHAN;

CAPRA HIRCUS; PICHIA PASTORIS;

EID: 19544362355     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20496     Document Type: Article

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